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Copper in PDB 2aps: Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae

Protein crystallography data

The structure of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae, PDB code: 2aps was solved by K.T.Forest, P.R.Langford, J.S.Kroll, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 58.050, 123.880, 107.250, 90.00, 90.00, 90.00
R / Rfree (%) 22.1 / 26.1

Copper Binding Sites:

The binding sites of Copper atom in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae (pdb code 2aps). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae, PDB code: 2aps:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2aps

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Copper binding site 1 out of 4 in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu300

b:41.4
occ:0.50
NE2 A:HIS50 1.7 57.3 1.0
NE2 A:HIS48 1.7 52.7 1.0
CE1 A:HIS50 2.5 58.1 1.0
CE1 A:HIS48 2.7 55.3 1.0
CD2 A:HIS48 2.8 54.2 1.0
CD2 A:HIS50 2.8 55.9 1.0
ND1 A:HIS50 3.6 59.3 1.0
ND1 A:HIS48 3.8 50.8 1.0
CG A:HIS50 3.8 56.3 1.0
CG A:HIS48 3.9 50.4 1.0

Copper binding site 2 out of 4 in 2aps

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Copper binding site 2 out of 4 in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu402

b:43.8
occ:1.00
NE2 A:HIS141 1.9 37.4 1.0
NE2 A:HIS62 2.2 46.7 1.0
ND1 A:HIS60 2.3 36.3 1.0
CE1 A:HIS141 2.8 41.5 1.0
NE2 A:HIS85 2.9 39.7 1.0
CD2 A:HIS141 3.0 41.2 1.0
CE1 A:HIS62 3.1 45.3 1.0
CE1 A:HIS60 3.2 34.7 1.0
CG A:HIS60 3.2 34.1 1.0
CD2 A:HIS62 3.3 46.8 1.0
CD2 A:HIS85 3.4 37.1 1.0
CB A:HIS60 3.5 33.1 1.0
CE1 A:HIS85 3.8 38.1 1.0
CB A:MET139 3.9 47.4 1.0
ND1 A:HIS141 3.9 39.9 1.0
CG A:MET139 4.0 50.6 1.0
CG A:HIS141 4.1 39.6 1.0
ND1 A:HIS62 4.3 47.4 1.0
NE2 A:HIS60 4.3 35.2 1.0
CD2 A:HIS60 4.3 34.7 1.0
CG A:HIS62 4.4 45.1 1.0
CG A:HIS85 4.4 39.1 1.0
CA A:HIS60 4.5 34.4 1.0
N A:HIS60 4.6 33.9 1.0
O A:HOH1271 4.6 47.3 1.0
ND1 A:HIS85 4.6 37.6 1.0
O A:HIS60 4.7 39.0 1.0
C A:HIS60 4.8 36.5 1.0
O A:MET139 4.9 43.0 1.0

Copper binding site 3 out of 4 in 2aps

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Copper binding site 3 out of 4 in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu500

b:32.4
occ:1.00
O B:HOH1353 1.5 32.4 1.0
NE2 B:HIS48 2.3 34.5 1.0
NE2 B:HIS50 2.3 24.1 1.0
CD2 B:HIS50 3.0 22.9 1.0
CE1 B:HIS48 3.1 35.8 1.0
CD2 B:HIS48 3.2 32.4 1.0
CE1 B:HIS50 3.5 24.0 1.0
ND1 B:HIS48 4.2 37.1 1.0
CG B:HIS50 4.2 22.7 1.0
CG B:HIS48 4.3 30.0 1.0
ND1 B:HIS50 4.4 26.9 1.0

Copper binding site 4 out of 4 in 2aps

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Copper binding site 4 out of 4 in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu602

b:26.6
occ:1.00
ND1 B:HIS60 2.0 21.3 1.0
NE2 B:HIS62 2.1 18.0 1.0
NE2 B:HIS141 2.1 23.9 1.0
CE1 B:HIS60 2.8 22.3 1.0
CE1 B:HIS62 3.0 19.1 1.0
NE2 B:HIS85 3.0 20.6 1.0
CD2 B:HIS141 3.0 21.6 1.0
CD2 B:HIS62 3.1 18.9 1.0
CG B:HIS60 3.1 21.2 1.0
O B:HOH1224 3.1 41.5 1.0
CE1 B:HIS141 3.1 22.1 1.0
CD2 B:HIS85 3.5 21.7 1.0
CB B:HIS60 3.6 20.6 1.0
CE1 B:HIS85 3.9 20.4 1.0
CB B:MET139 3.9 20.2 1.0
NE2 B:HIS60 4.0 25.2 1.0
CG B:MET139 4.0 22.7 1.0
ND1 B:HIS62 4.1 19.7 1.0
CD2 B:HIS60 4.1 19.6 1.0
CG B:HIS141 4.2 18.6 1.0
CG B:HIS62 4.2 21.5 1.0
ND1 B:HIS141 4.2 18.7 1.0
O B:HOH1223 4.3 25.4 1.0
CG B:HIS85 4.4 22.1 1.0
CA B:HIS60 4.5 19.7 1.0
N B:HIS60 4.5 21.1 1.0
ND1 B:HIS85 4.6 21.4 1.0
O B:HIS60 4.7 18.2 1.0
C B:HIS60 4.8 20.7 1.0
O B:MET139 4.9 19.9 1.0

Reference:

K.T.Forest, P.R.Langford, J.S.Kroll, E.D.Getzoff. Cu,Zn Superoxide Dismutase Structure From A Microbial Pathogen Establishes A Class with A Conserved Dimer Interface. J.Mol.Biol. V. 296 145 2000.
ISSN: ISSN 0022-2836
PubMed: 10656823
DOI: 10.1006/JMBI.1999.3448
Page generated: Thu Sep 3 16:29:25 2020
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